Biochemical studies of phenoloxidase and utilization of catecholamines in Cryptococcus neoformans.
Protoplasts of Cryptococcus neoformans contain phenoloxidase as a membrane-bound enzyme. The enzyme appeared to be attached on the inner side of cytoplasmic membranes. Synthesis of the enzyme was derepressed by low levels of glucose but was not affected by the level of ammonium. Copper chelators which inhibited the phenoloxidase of other organisms did not affect cryptococcal enzymes. However, cyanide- or iron-chelating agents such as hydroximide derivates or 8-hydroxyquinoline were effective inhibitors, suggesting that cryptococcal phenoloxidase is an iron-containing enzyme. Phenoloxidase of C. neoformans catalyzed the oxidation of various diphenols via dopachrome and labile intermediates to melanin polymers. The kinetic constants (Km) of the phenoloxidase and the permease for dopamine and norepinephrine were low. The correlation between phenoloxidase and the preferential growth of C. neoformans in the host brain is discussed.
D000641:Ammonia / Q000494:pharmacology; D004156:Catechol Oxidase / Q000378:metabolism*; D002395:Catecholamines / Q000378:metabolism*; D002413:Cations, Divalent / Q000494:pharmacology; D003454:Cryptococcus / Q000201:enzymology*; D003455:Cryptococcus neoformans / Q000201:enzymology*; D005947:Glucose / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D012995:Solubility; D013379:Substrate Specificity; D013696:Temperature
D002395:Catecholamines; D002413:Cations, Divalent; D000641:Ammonia; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase; D005947:Glucose